ID   ACHN3_CARAU             Reviewed;         466 AA.
AC   P18257;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Neuronal acetylcholine receptor subunit non-alpha-3;
DE   AltName: Full=GFN-alpha-3;
DE   Flags: Precursor;
OS   Carassius auratus (Goldfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Carassius.
OX   NCBI_TaxID=7957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retina;
RX   PubMed=2303867; DOI=10.1523/jneurosci.10-02-00670.1990;
RA   Cauley K., Agranoff B.W., Goldman D.;
RT   "Multiple nicotinic acetylcholine receptor genes are expressed in goldfish
RT   retina and tectum.";
RL   J. Neurosci. 10:670-683(1990).
CC   -!- FUNCTION: After binding acetylcholine, the AChR responds by an
CC       extensive change in conformation that affects all subunits and leads to
CC       opening of an ion-conducting channel across the plasma membrane.
CC   -!- SUBUNIT: Neuronal AChR seems to be composed of two different type of
CC       subunits: alpha and non-alpha (beta).
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC       protein. Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Retina, tectum and brain.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC       Acetylcholine receptor (TC 1.A.9.1) subfamily. {ECO:0000305}.
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DR   EMBL; M29529; AAA49167.1; -; mRNA.
DR   PIR; S16333; S16333.
DR   AlphaFoldDB; P18257; -.
DR   SMR; P18257; -.
DR   Proteomes; UP000515129; Genome assembly.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IEA:InterPro.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   Gene3D; 1.20.58.390; -; 2.
DR   Gene3D; 2.70.170.10; -; 1.
DR   InterPro; IPR006202; Neur_chan_lig-bd.
DR   InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR   InterPro; IPR006201; Neur_channel.
DR   InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR   InterPro; IPR038050; Neuro_actylchol_rec.
DR   InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR   InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR   InterPro; IPR002394; Nicotinic_acetylcholine_rcpt.
DR   PANTHER; PTHR18945; PTHR18945; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 1.
DR   PRINTS; PR00254; NICOTINICR.
DR   PRINTS; PR00252; NRIONCHANNEL.
DR   SUPFAM; SSF63712; SSF63712; 1.
DR   SUPFAM; SSF90112; SSF90112; 1.
DR   TIGRFAMs; TIGR00860; LIC; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW   Ligand-gated ion channel; Membrane; Postsynaptic cell membrane; Receptor;
KW   Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix;
KW   Transport.
FT   SIGNAL          1..28
FT   CHAIN           29..466
FT                   /note="Neuronal acetylcholine receptor subunit non-alpha-3"
FT                   /id="PRO_0000000394"
FT   TOPO_DOM        29..235
FT                   /note="Extracellular"
FT   TRANSMEM        236..260
FT                   /note="Helical"
FT   TRANSMEM        268..285
FT                   /note="Helical"
FT   TRANSMEM        302..323
FT                   /note="Helical"
FT   TOPO_DOM        324..438
FT                   /note="Cytoplasmic"
FT   TRANSMEM        439..456
FT                   /note="Helical"
FT   CARBOHYD        54
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        208
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        156..170
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   466 AA;  53802 MW;  3EED8C870CC9B5F8 CRC64;
     MKLQISGLLL VTAVAYATIE APEEFVSLAE MEDTLLRNLF RGYQKWVRPI LHANDTITVR
     FGLKISQLVD VDEKNHLMTT NVWLWQEWTD YKLRWNPEDY GGITSIRVPS ETIWLPDIVL
     YENADGRFEG SLMTKAIVRF NGTIMWTPPA SYKSSCTMDV TFFPFDRQNC SMKFGSWTYD
     GTMVDLTLLD AYVDRKDFFD NGEWEILNAT GQRGSRRDGI YSYPYVTYSF ILKRLPLFYT
     LFLIIPCLGL SFLTVLVFYL PSDEGEKLLL STSVLVSLTV FLLVIEEIIP SSSKVIPLIG
     EYLLFIMIFV TFSIIVTLFV INVHHRSSAT YHPMAPWVKS LFLQRLPRLL CMRGHTDRYQ
     YPDIELRSPE LKRGMKKGQQ KSAGGGRGGL KEDENQAWIA LLEKATHSVH YISRHIKKEH
     FIREVVQDWK FVAQVLDRIF LWVFLTASVL GTILIFTPAL HMYLST